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J Biol Chem. 2015 May 8;290(19):12147-64. doi: 10.1074/jbc.M115.637694. Epub 2015 Mar 23.

The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain.

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From the Divisions of Parasitology.
the School of Life Sciences, Queens Medical Centre, University of Nottingham, Nottingham NG2 7UH, United Kingdom.
the Institute of Cell Biology, University of Bern, CH-3012 Bern, Switzerland, and.
Physical Biochemistry, and.
Molecular Structure, MRC National Institute for Medical Research, London NW7 1AA, United Kingdom.
the Institute of Chemical Biology, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
From the Divisions of Parasitology,


Myosin B (MyoB) is one of the two short class XIV myosins encoded in the Plasmodium genome. Class XIV myosins are characterized by a catalytic "head," a modified "neck," and the absence of a "tail" region. Myosin A (MyoA), the other class XIV myosin in Plasmodium, has been established as a component of the glideosome complex important in motility and cell invasion, but MyoB is not well characterized. We analyzed the properties of MyoB using three parasite species as follows: Plasmodium falciparum, Plasmodium berghei, and Plasmodium knowlesi. MyoB is expressed in all invasive stages (merozoites, ookinetes, and sporozoites) of the life cycle, and the protein is found in a discrete apical location in these polarized cells. In P. falciparum, MyoB is synthesized very late in schizogony/merogony, and its location in merozoites is distinct from, and anterior to, that of a range of known proteins present in the rhoptries, rhoptry neck or micronemes. Unlike MyoA, MyoB is not associated with glideosome complex proteins, including the MyoA light chain, myosin A tail domain-interacting protein (MTIP). A unique MyoB light chain (MLC-B) was identified that contains a calmodulin-like domain at the C terminus and an extended N-terminal region. MLC-B localizes to the same extreme apical pole in the cell as MyoB, and the two proteins form a complex. We propose that MLC-B is a MyoB-specific light chain, and for the short class XIV myosins that lack a tail region, the atypical myosin light chains may fulfill that role.


Invasion; Malaria; Molecular Motor; Myosin; Myosin Light Chain; Parasite; Peptide Interaction; Plasmodium

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